Dynamics and conformation of polypeptides

✍ Scribed by V. D. Gupta

• Book ID: 104580326
• Publisher: John Wiley and Sons
• Year: 1981
• Tongue: English
• Weight: 590 KB
• Volume: 20
• Category: Article
• ISSN: 0020-7608
• DOI: 10.1002/qua.560200102

✦ Synopsis

Abstract

The dynamics of simple polypeptides is studied both from theoretical and experimental viewpoints. Theoretically, dispersion curves and frequency distributions are obtained from Wilson's GF matrix method as modified by Higgs for an infinite helical system. The systems studied are polyglycine I and polyglycine II, polyalanine in α and α forms, poly‐L‐proline I and poly‐L‐proline II, and poly‐L‐hydroxyproline. Conformation sensitive modes and their dispersion in the BZ are reported. In several of these, the results are compared with the measurements from inelastic neutron scattering. Since the neutrons have a large incoherent scattering cross section for hydrogen, it enables us to examine a normal mode via the motion of protons involved. In addition, neutron scattering is not controlled by symmetry dependent “selection rules.” Conformational studies of oligomers of glycine, alanine, and proline in relation to their polymeric forms as deduced from the dispersion curves and spectroscopic studies are presented. Recent measurements on the specific heat of polyglycine and polyalanine by Finegold et al. are also reported.